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Study Guide Exam 2

by: Michael Notetaker

Study Guide Exam 2 BISC207

Michael Notetaker
GPA 3.895

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Topics 4, 5, and 6
Study Guide
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This 4 page Study Guide was uploaded by Michael Notetaker on Sunday March 20, 2016. The Study Guide belongs to BISC207 at University of Delaware taught by JaneNoble-Harvey in Spring 2016. Since its upload, it has received 42 views. For similar materials see Biology in Biological Sciences at University of Delaware.


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Date Created: 03/20/16
Ryan Cleary Exam 2 Study Guide Topic 4 • 20 amino acids all of which have different R-function groups o Hydrophobic-hydrocarbon chain or ring o Hydrophilic-basic, acidic, or polar o Special-glycine (only H as R), proline (creates ring with alpha and amine group), and cysteine (CH SH group source of sulfur, spontaneous reaction 2 with two cysteine and lose H’s on end and form disulfide bond) • Gene determines sequence of amino acids in polypeptide chain • Alpha helix-held together in helix structure by O-H H-bonding interaction form backbone (primary) • Beta sheet-adjacent strands lining up parallel to each other and O-H H-bonding interactions (like folded paper) (secondary) • Other twists and turns occur in amino acid from the charges or the R-functional group that are weaker interactions (tertiary structure) • Interactions occur between different chains in hemoglobin (quaternary structure) • Translation-RNA à protein, ribosomes are large and small subunits • tRNA-codon carries genetic information for 1 amino acid, tRNA carries anticodon which is 3 bases and it’s the adaptor between RNA and proteins • Aminoacyl tRNA synthetase enzymes o 3 base pairs on tRNA leads to the determination of which enzyme will be added to tRNA o Aminoacyl tRNA synthetase binds one amino acid to tRNA based on which bases are present • Standard genetic code-code in mRNA leads to the production and attaching of the corresponding amino acid to the tRNA o Stop codon-UGA, UAA, UAG o Start codon-AUG o Genetic codon is degenerate (more than one code standing for an amino acid) • Monocistronic mRNA-one gene being represented • Creation of protein o Initiation factors at 5’ end and bring up tRNA o Complex scans for AUG o Initiation factors are released and large subunit joins complex and the next tRNA is added to A site o Peptidyl transferase-ribozyme, transfers amino acid from left tRNA to the right tRNA so the two amino acids forming peptidic bonds o Stop codon has release factor on tRNA and the amino acid is released Topic 5 • Hooke first saw divided areas and said they looked like cells that monks lived in • All organisms are made up of cells • Cells form from preexisting cells • Cell is the fundamental unit of life • Phospholipid bilayer o Lipid structure in water: micelle à bilayer à liposome (vesicle) o Cholesterol-hydrophilic head (OH), rigid planar group of rings, and hydrophobic hydrocarbon tail o Transport-lets in molecules into cell, channels allow free flow and carriers alter their shape to allow bigger molecules in o Receptor-picks up signal molecules and sends information into cell, allows cells to respond to changes outside the cell o Enzyme-can catalyze reaction of the outside of the cell o Integral membrane-transmembrane proteins that span the entire membrane o Peripheralmembrane1972-proteins that are temporarily associated with the internal and external side of the membrane (proteins that are anchored) o Proteins are able to move around in the plane of the membrane o 1972 Fluid Mosaic Model-lipids and proteins coexist in membrane, molecules move laterally in membrane, so the membrane is “fluid” o Outside of the membrane has carbohydrates attached to proteins and lipids detect signals • Transport o Diffusion-movement of solute from high concentration to low concentration until concentrations are equal o Simple diffusion-small molecules flowing through the membrane/lipid bilayer always from high to low concentration o Passive diffusion-diffusion that requires no energy from the cell o Active diffusion-diffusion that requires energy from the cell o Channel-mediated diffusion-facilitated diffusion where polar molecules can flow through a channel from high to low concentrations (passive) o Carrier-mediated- facilitated diffusion where polar molecules can flow through a carrier from high to low concentrations (passive) o Osmosis-water flows from areas of low solute concentration to areas of high solute concentration to balance concentration o Cells work to create concentration gradient in order to create potential energy o Primary active transport-Na binds to the transport sites on enzyme/carrier and ATP binds to carrier and flips the structure/configuration which allows + + the Na to be released from the cell, K from outside the cell binds to the other side of the carrier and the ATP is released flipping the carrier back to its original configuration and the K is released into the cell creating a gradient with Na on the outside and K on the inside (active) o Secondary active transport-using gradient in primary active transport to dump useless material as we move Na and K with gradient, protons are pumped out of the cell to create gradient, moving along gradient can act as antiporter and transport different molecules out of the cell against gradient, phosphate group that interacts with protein and negative charge alters protein’s structure, ATP is only required to create gradient • Simple transport-water goes through cell membrane with assistance of protein • Facilitated transfusion-molecules go through specific proteins into the cell, requires no energy • Na -K ATPase-pumps Na out and K in and interacts with ATP to break it down, enzyme creates gradient • Plasma is isotonic to red blood cells o Cell will shrink in hypertonic (highly concentrated) solution, fatal o Cell will expand in hypotonic (lowly concentrated) solution, fatal (lysis) • Plant cells absorb water until the plasma membrane pushes against the cell wall, plant will stand straight up when vacuoles are filled • Dehydrated plants cells collapse vacuoles and die • Prokaryotic cells are 1/10 the size of eukaryotic cells • Parts of animal cells o Endomembrane system-organelles that link to nucleus, connected physically and by means of vesicles § Nuclear envelop and endoplasmic reticulum § Endoplasmic reticulum can bud and can send vesicles to Golgi apparatus § During division of nucleus/cell division, nuclear envelop turns into vesicles and moves to cytoplasm o Rough endoplasmic reticulum-ribosomes are attached o Smooth endoplasmic reticulum-tubular o Cytosol-water substance around nucleus o Cytoplasm-everything that is not the nucleus in the cell o Proteins made by ribosomes on rough ER are used outside the cell while proteins made on the ribosomes in the cytosol are used in the cell • EMS-endomembrane system o Nuclear envelop o Endoplasmic reticulum o Golgi apparatus • Protein is thread through ribosomes on rough ER and into lumen (membrane sacks) • Two spaces in a cell-cytoplasm/cytosol and lumen membrane • Golgi apparatus-processes the products coming from the smooth and rough ER, vesicles break off and can be taken out of the cell (exocytosis) • Endocytosis vesicles enter cell while exocytosis vesicles leave the cell • Lysosomes-acts as a digestive system in the cell, acid hydrolase is the enzyme, acts to add water to bonds to break them, has proton pump to adjust pH, waste exits cell through exocytosis • Secretory protein pathway-Rough ER à Golgi apparatus à vesicle à exocytosis • Entry into RER lumen-amino acid terminal binds with SRP and gives signal to RER and protein moves into lumen and signal sequence (amino acid) is cleaved • Mitochondria-has inner and outer membrane, aqueous compartment between • Chloroplasts-only in plant cells, site of photosynthesis, inner, outer, and thylakoid (where photosynthesis occurs) membranes Topic 6 • Cells have the ability to do work, mostly from chemical energy in ATP • ATP-adenosine 5’-triphosphate • Chemotrophs make their own food (carbon from CO ) whi2e autotrophs eat their food (carbon from organic compounds) • Metabolism-all chemical reactions of an organism or a cell o The break down of organic compounds to release energy (catabolism) and building of organic molecules which harnesses energy (anabolism) • The further the electron is away from the nucleus the more potential energy it has • Total energy=energy available to do work + energy lost to entropy (disorder/heat) à H = G + TS o Endergonic reaction-nonspontaneous reaction (+∆G), energy is needed for reaction o Exergonic reaction-spontaneous reaction (-∆G), energy released from reaction o Reactions can be coupled with other reactions in order to allow nonspontaneous reactions to occur • To make new bonds, breaking bonds requires energy (activation energy) and catalyst can lower that energy • Enzymes react with substrate to produce Enzyme Substrate à Enzyme Product à Enzyme + Product, enzyme breaks away from new product because the structure isn’t right and breaks away unchanged • Proteins/enzymes have weak bonds and weak IMF’s so they will denature under change in temperature of change in pH • Allosteric inhibition-“another space” on the enzyme • Competitive inhibitor-enzyme binds to substrate and makes product or inhibitor • Non-competitive inhibitor-binds to another site on the enzyme and doesn’t allow the enzyme to complete the reaction even if it binds to the substrate


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